8wg3

mouse TMEM63b in LMNG-CHS micelle

Method: ELECTRON MICROSCOPY Dmax: 95.3 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

CSC1-like protein 2,Green fluorescent protein

Aequorea victoria

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–238 Mutation:F64L,S65T,A206K,H231L Non-standard monomer:Yes (specific site not provided by mmCIF) Y01 CHOLESTEROL HEMISUCCINATE × 3 LBN 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 848–1084; UniProt 2–238

CSC1-like protein 2,Green fluorescent protein

Aequorea victoria

UniProt Q3TWI9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–832 Mutation:F64L,S65T,A206K,H231L Non-standard monomer:Yes (specific site not provided by mmCIF) Y01 CHOLESTEROL HEMISUCCINATE × 3 LBN 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSCL2_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–832; UniProt 1–832

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8wg3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8wg3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8wg3
Deposition date deposition_date2023-09-20
Structure title titlemouse TMEM63b in LMNG-CHS micelle
Keywords keywordsScramblase, LIPID TRANSPORT; LIPID TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier28.70
Radius of gyration Rg (electron density) rg_electron27.42
Forward intensity I(0) i054836800.00
Molecular weight molecular_weight65012.0 kDa
Excluded volume excluded_volume84386 ų
Envelope volume envelope_volume105720 ų
Hydration-shell volume shell_volume32731 ų
Envelope diameter envelope_diameter100.7
Shell Rg shell_rg34.18
Envelope Rg envelope_rg27.81
Shape Rg shape_rg27.42
Total Rg total_rg28.20
Total atoms total_atoms4585
Residues n_residues547
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax95.3
Rg (real space) rg_real28.75
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real5.4840e+07
I(0) uncertainty (real space) i0_real_error8.8850e+05
Rg (reciprocal space) rg_reciprocal28.73
I(0) (reciprocal space) i0_reciprocal54840000.0000
Solution quality estimate total_estimate0.8892
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.2
Skewness Skewness skewness0.369
Kurtosis Kurtosis kurtosis-0.393
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7717000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.930; Smooth: 0.947

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)